Laparoscopic radical hysterectomy with lymphadenectomy in patients with early cervical cancer: Our instruments and technique
SURGICAL ONCOLOGY-OXFORD
Authors: Malzoni, Mario; Tinelli, Raffaele; Cosentino, Francesco; Perone, Ciro; Iuzzolino, Domenico; Rasile, Marianna; Tinelli, Andrea
Abstract
The purpose of this study is to describe the technique of total laparoscopic radical hysterectomy (type III procedure) with lymphadenectomy as performed at the Advanced Gynecological Endoscopy Center of the Malzoni Medical Center, Avellino, Italy. Seventy-seven patients underwent total laparoscopic radical hysterectomy (type 11, 111) with lymphadenectomy between January 2000 and March 2008. FIGO stage included five patients Ia1 with LVSI (lymph-vascular involvement), 24 patients Ia2, and 48 patients Ib1. 60 patients underwent a class III procedure and 17 patients a class II procedure according to the Piver classification. Histological types included squamous cell carcinoma in 65 patients, adenocarcinomas in 10 patients, and adenosquamous carcinoma in two. Para-aortic lymphadenectomy was performed up to the level of the inferior mesenteric artery in eight cases with positive pelvic lymph nodes at frozen section evaluation. Total laparoscopic radical hysterectomy can be considered a safe and effective therapeutic procedure for the management of early stage cervical cancer with a low morbidity; moreover, the laparoscopic route may offer an alternative option for patients undergoing radical hysterectomy, although multicenter studies and tong-term follow-up are required to evaluate the oncologic outcomes of this procedure. (C) 2008 Elsevier Ltd. All rights reserved.
Improved expression and characterization of recombinant human Golgi alpha 1, 2-mannosidase I isoforms (IA2 and IC) by Escherichia coli
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
Authors: Isoyama-Tanaka, Junko; Dohi, Koji; Misaki, Ryo; Fujiyama, Kazuhito
Abstract
Golgi alpha 1,2-mannosidase I is involved in the N-linked oligosaccharide processing pathway. In this study, two truncated genes encoding for human Golgi alpha 1,2-mannosidase I (hManIA2: amino acids 127-626 and hManIC: amino acids 118-617) were expressed in Escherichia coli to characterize the enzymes. These genes were fused to a 17 protein tag and a histidine tag at the N- and C-terminal ends, respectively, and purified using Co2+ affinity chromatography. The properties including optimal temperature, optimal pH, and substrate specificity of the purified enzymes were investigated by HPLC using pyridylamino (PA)-labeled oligosaccharides as substrates. The stability of hManIA2 was dependent on the presence of Ca2+, which was also required for its activity. On the other hand, hManIC was stable in the absence of Ca2+, even though Ca2+ was also effective for the activity of hManIC. While the similarity of the amino acid sequences is over 60%, hManIA2 and hManIC showed different substrate specificities particularly toward M9A and M8C. (C) 2011, The Society for Biotechnology, Japan. All rights reserved.